RL2_DEIRA
ID RL2_DEIRA Reviewed; 275 AA.
AC Q9RXJ9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=50S ribosomal protein L2;
GN Name=rplB; OrderedLocusNames=DR_0314;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, AND PROTEIN
RP SEQUENCE OF 1-6.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11733066; DOI=10.1016/s0092-8674(01)00546-3;
RA Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I.,
RA Bartels H., Franceschi F., Yonath A.;
RT "High resolution structure of the large ribosomal subunit from a mesophilic
RT eubacterium.";
RL Cell 107:679-688(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11677599; DOI=10.1038/35101544;
RA Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R.,
RA Yonath A., Franceschi F.;
RT "Structural basis for the interaction of antibiotics with the peptidyl
RT transferase centre in eubacteria.";
RL Nature 413:814-821(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TRNA MIMICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12535524; DOI=10.1016/s1097-2765(03)00009-1;
RA Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R.,
RA Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E., Kessler M.,
RA Yonath A.;
RT "Structural basis of the ribosomal machinery for peptide bond formation,
RT translocation, and nascent chain progression.";
RL Mol. Cell 11:91-102(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP MODIFIED MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12623020; DOI=10.1016/s0969-2126(03)00022-4;
RA Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H.,
RA Zarivach R., Yonath A.;
RT "Structural basis for the antibiotic activity of ketolides and azalides.";
RL Structure 11:329-338(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TROLEANDOMYCIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12665853; DOI=10.1038/nsb915;
RA Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D.,
RA Yonath A.;
RT "Structural insight into the role of the ribosomal tunnel in cellular
RT regulation.";
RL Nat. Struct. Biol. 10:366-370(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15059283; DOI=10.1186/1741-7007-2-4;
RA Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A.;
RT "Alterations at the peptidyl transferase centre of the ribosome induced by
RT the synergistic action of the streptogramins dalfopristin and
RT quinupristin.";
RL BMC Biol. 2:4-4(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP TIAMULIN.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15554968; DOI=10.1111/j.1365-2958.2004.04346.x;
RA Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M.;
RT "Inhibition of peptide bond formation by pleuromutilins: the structure of
RT the 50S ribosomal subunit from Deinococcus radiodurans in complex with
RT tiamulin.";
RL Mol. Microbiol. 54:1287-1294(2004).
CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF09895.1; -; Genomic_DNA.
DR PIR; B75534; B75534.
DR RefSeq; NP_294037.1; NC_001263.1.
DR RefSeq; WP_010886959.1; NZ_CP015081.1.
DR PDB; 1NKW; X-ray; 3.10 A; A=1-275.
DR PDB; 1NWX; X-ray; 3.50 A; A=2-275.
DR PDB; 1NWY; X-ray; 3.30 A; A=2-275.
DR PDB; 1SM1; X-ray; 3.42 A; A=1-275.
DR PDB; 1XBP; X-ray; 3.50 A; A=2-275.
DR PDB; 2ZJP; X-ray; 3.70 A; A=2-275.
DR PDB; 2ZJQ; X-ray; 3.30 A; A=2-275.
DR PDB; 2ZJR; X-ray; 2.91 A; A=2-275.
DR PDB; 3CF5; X-ray; 3.30 A; A=2-275.
DR PDB; 3DLL; X-ray; 3.50 A; A=2-275.
DR PDB; 3PIO; X-ray; 3.25 A; A=2-275.
DR PDB; 3PIP; X-ray; 3.45 A; A=2-274.
DR PDB; 4IO9; X-ray; 3.20 A; A=2-275.
DR PDB; 4IOA; X-ray; 3.20 A; A=2-275.
DR PDB; 4IOC; X-ray; 3.60 A; A=2-275.
DR PDB; 4U67; X-ray; 3.65 A; A=1-275.
DR PDB; 4V49; X-ray; 8.70 A; A=4-273.
DR PDB; 4V4A; X-ray; 9.50 A; A=4-273.
DR PDB; 4V4G; X-ray; 11.50 A; D=4-273.
DR PDB; 4WFN; X-ray; 3.54 A; A=1-275.
DR PDB; 5DM6; X-ray; 2.90 A; A=2-275.
DR PDB; 5DM7; X-ray; 3.00 A; A=2-275.
DR PDB; 5JVG; X-ray; 3.43 A; A=1-275.
DR PDB; 5JVH; X-ray; 3.58 A; A=1-275.
DR PDB; 7A0R; X-ray; 3.30 A; A=2-272.
DR PDB; 7A0S; X-ray; 3.22 A; A=2-275.
DR PDB; 7A18; X-ray; 3.40 A; A=2-272.
DR PDBsum; 1NKW; -.
DR PDBsum; 1NWX; -.
DR PDBsum; 1NWY; -.
DR PDBsum; 1SM1; -.
DR PDBsum; 1XBP; -.
DR PDBsum; 2ZJP; -.
DR PDBsum; 2ZJQ; -.
DR PDBsum; 2ZJR; -.
DR PDBsum; 3CF5; -.
DR PDBsum; 3DLL; -.
DR PDBsum; 3PIO; -.
DR PDBsum; 3PIP; -.
DR PDBsum; 4IO9; -.
DR PDBsum; 4IOA; -.
DR PDBsum; 4IOC; -.
DR PDBsum; 4U67; -.
DR PDBsum; 4V49; -.
DR PDBsum; 4V4A; -.
DR PDBsum; 4V4G; -.
DR PDBsum; 4WFN; -.
DR PDBsum; 5DM6; -.
DR PDBsum; 5DM7; -.
DR PDBsum; 5JVG; -.
DR PDBsum; 5JVH; -.
DR PDBsum; 7A0R; -.
DR PDBsum; 7A0S; -.
DR PDBsum; 7A18; -.
DR AlphaFoldDB; Q9RXJ9; -.
DR SMR; Q9RXJ9; -.
DR DIP; DIP-58602N; -.
DR IntAct; Q9RXJ9; 2.
DR STRING; 243230.DR_0314; -.
DR EnsemblBacteria; AAF09895; AAF09895; DR_0314.
DR KEGG; dra:DR_0314; -.
DR PATRIC; fig|243230.17.peg.480; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_0; -.
DR InParanoid; Q9RXJ9; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR EvolutionaryTrace; Q9RXJ9; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..275
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129558"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:7A0S"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7A0S"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:5JVG"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4IO9"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3CF5"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3DLL"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7A18"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:7A18"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5DM7"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4IO9"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2ZJR"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3PIO"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4IO9"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:5DM6"
SQ SEQUENCE 275 AA; 30045 MW; A96E5853B592C11E CRC64;
MAVKKYRPYT PSRRQMTTAD FSGLTKKRPE KALTEALPKT GGRNNRGRIT SRFIGGGHKR
LYRIIDFKRR DKSGVNAKVA AIEYDPNRSA RIALLHYADG EKRYILAPEG LTVGATVNAG
PEAEPKLGNA LPLRFVPVGA VVHALELVPG KGAQLARSAG TSVQVQGKES DYVIVRLPSG
ELRRVHSECY ATIGAVGNAE HKNIVLGKAG RSRWLGRKPH QRGSAMNPVD HPHGGGEGRT
GAGRVPVTPW GKPTKGLKTR RKRKTSDRFI VTRRK
